A novel role of the ferric reductase Cfl1 in cell wall integrity, mitochondrial function, and invasion to host cells in Candida albicans. Issue 7 (28th August 2014)
- Record Type:
- Journal Article
- Title:
- A novel role of the ferric reductase Cfl1 in cell wall integrity, mitochondrial function, and invasion to host cells in Candida albicans. Issue 7 (28th August 2014)
- Main Title:
- A novel role of the ferric reductase Cfl1 in cell wall integrity, mitochondrial function, and invasion to host cells in Candida albicans
- Authors:
- Yu, Qilin
Dong, Yijie
Xu, Ning
Qian, Kefan
Chen, Yulu
Zhang, Biao
Xing, Laijun
Li, Mingchun - Abstract:
- <abstract abstract-type="main" id="fyr12194-abs-0001"> <title>Abstract</title> <p> <italic>Candida albicans</italic> is an important opportunistic pathogen, causing both superficial mucosal infections and life‐threatening systemic diseases. Iron acquisition is an important factor for pathogen–host interaction and also a significant element for the pathogenicity of this organism. Ferric reductases, which convert ferric iron into ferrous iron, are important components of the high‐affinity iron uptake system. Sequence analyses have identified at least 17 putative ferric reductase genes in <italic>C. albicans</italic> genome. <italic>CFL1</italic> was the first ferric reductase identified in <italic>C. albicans</italic>. However, little is known about its roles in <italic>C. albicans</italic> physiology and pathogenicity. In this study, we found that disruption of <italic>CFL1</italic> led to hypersensitivity to chemical and physical cell wall stresses, activation of the cell wall integrity (CWI) pathway, abnormal cell wall composition, and enhanced secretion, indicating a defect in CWI in this mutant. Moreover, this mutant showed abnormal mitochondrial activity and morphology, suggesting a link between ferric reductases and mitochondrial function. In addition, this mutant displayed decreased ability of adhesion to both the polystyrene microplates and buccal epithelial cells and invasion of host epithelial cells. These findings revealed a novel role of<abstract abstract-type="main" id="fyr12194-abs-0001"> <title>Abstract</title> <p> <italic>Candida albicans</italic> is an important opportunistic pathogen, causing both superficial mucosal infections and life‐threatening systemic diseases. Iron acquisition is an important factor for pathogen–host interaction and also a significant element for the pathogenicity of this organism. Ferric reductases, which convert ferric iron into ferrous iron, are important components of the high‐affinity iron uptake system. Sequence analyses have identified at least 17 putative ferric reductase genes in <italic>C. albicans</italic> genome. <italic>CFL1</italic> was the first ferric reductase identified in <italic>C. albicans</italic>. However, little is known about its roles in <italic>C. albicans</italic> physiology and pathogenicity. In this study, we found that disruption of <italic>CFL1</italic> led to hypersensitivity to chemical and physical cell wall stresses, activation of the cell wall integrity (CWI) pathway, abnormal cell wall composition, and enhanced secretion, indicating a defect in CWI in this mutant. Moreover, this mutant showed abnormal mitochondrial activity and morphology, suggesting a link between ferric reductases and mitochondrial function. In addition, this mutant displayed decreased ability of adhesion to both the polystyrene microplates and buccal epithelial cells and invasion of host epithelial cells. These findings revealed a novel role of <italic>C. albicans</italic> Cfl1 in maintenance of CWI, mitochondrial function, and interaction between this pathogen and the host.</p> </abstract> … (more)
- Is Part Of:
- FEMS yeast research. Volume 14:Issue 7(2014)
- Journal:
- FEMS yeast research
- Issue:
- Volume 14:Issue 7(2014)
- Issue Display:
- Volume 14, Issue 7 (2014)
- Year:
- 2014
- Volume:
- 14
- Issue:
- 7
- Issue Sort Value:
- 2014-0014-0007-0000
- Page Start:
- 1037
- Page End:
- 1047
- Publication Date:
- 2014-08-28
- Subjects:
- Yeast -- Periodicals
Yeasts -- Periodicals
579.562 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1567-1364 ↗
http://www.sciencedirect.com/science/journal/15671356 ↗
http://www.blackwell-synergy.com/rd.asp?goto=journal&code=fyr ↗
http://onlinelibrary.wiley.com/ ↗
http://femsyr.oxfordjournals.org/content/ ↗ - DOI:
- 10.1111/1567-1364.12194 ↗
- Languages:
- English
- ISSNs:
- 1567-1356
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.325000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4305.xml